ECFA1_LEUMM
ID ECFA1_LEUMM Reviewed; 272 AA.
AC Q03ZL6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710};
DE Short=ECF transporter A component EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_01710};
GN Name=ecfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO1, ecfA;
GN OrderedLocusNames=LEUM_0225;
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
RN [2]
RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION,
RP SUBSTRATES, AND EXPRESSION IN E.COLI.
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX PubMed=18931129; DOI=10.1128/jb.01208-08;
RA Rodionov D.A., Hebbeln P., Eudes A., ter Beek J., Rodionova I.A.,
RA Erkens G.B., Slotboom D.J., Gelfand M.S., Osterman A.L., Hanson A.D.,
RA Eitinger T.;
RT "A novel class of modular transporters for vitamins in prokaryotes.";
RL J. Bacteriol. 191:42-51(2009).
RN [3]
RP FUNCTION AS A TRANSPORT COMPONENT, SUBCELLULAR LOCATION, SUBUNIT, AND
RP EXPRESSION IN E.COLI.
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX PubMed=19717603; DOI=10.1128/jb.00965-09;
RA Neubauer O., Alfandega A., Schoknecht J., Sternberg U., Pohlmann A.,
RA Eitinger T.;
RT "Two essential arginine residues in the T components of energy-coupling
RT factor transporters.";
RL J. Bacteriol. 191:6482-6488(2009).
CC -!- FUNCTION: ATP-binding (A) component of a common energy-coupling factor
CC (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF
CC transporter provides the energy necessary to transport a number of
CC different substrates including 5-formyltetrahydrofolate, pantothenate
CC and riboflavin. Expression of the complex plus FolT in E.coli allows 5-
CC formyltetrahydrofolate uptake; 5-formyltetrahydrofolate is not taken up
CC in the absence of FolT or the EcfA1A2T complex. {ECO:0000255|HAMAP-
CC Rule:MF_01710, ECO:0000269|PubMed:18931129,
CC ECO:0000269|PubMed:19717603}.
CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC complex probably composed of 2 membrane-embedded substrate-binding
CC proteins (S component), 2 ATP-binding proteins (A component) and 2
CC transmembrane proteins (T component). This complex interacts with a
CC number of substrate-specific components, including FolT, PanT and RibU
CC for 5-formyltetrahydrofolate, pantothenate and riboflavin respectively.
CC {ECO:0000269|PubMed:18931129, ECO:0000269|PubMed:19717603}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:18931129,
CC ECO:0000305|PubMed:19717603}; Peripheral membrane protein
CC {ECO:0000305|PubMed:18931129, ECO:0000305|PubMed:19717603}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy-coupling
CC factor EcfA family. {ECO:0000255|HAMAP-Rule:MF_01710}.
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DR EMBL; CP000414; ABJ61356.1; -; Genomic_DNA.
DR RefSeq; WP_010282672.1; NC_008531.1.
DR AlphaFoldDB; Q03ZL6; -.
DR SMR; Q03ZL6; -.
DR STRING; 203120.LEUM_0225; -.
DR EnsemblBacteria; ABJ61356; ABJ61356; LEUM_0225.
DR GeneID; 61177296; -.
DR KEGG; lme:LEUM_0225; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_1_22_9; -.
DR OMA; RMKDFDA; -.
DR OrthoDB; 1713578at2; -.
DR Proteomes; UP000000362; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR InterPro; IPR030947; EcfA_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR04520; ECF_ATPase_1; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51246; CBIO; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Translocase;
KW Transport.
FT CHAIN 1..272
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA1"
FT /id="PRO_0000287961"
FT DOMAIN 5..239
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
SQ SEQUENCE 272 AA; 30282 MW; B463BE51F7ABD1D4 CRC64;
MVKAIKIDNL KYSYDERSLF SDFNLDIDAG QWVALVGHNG SGKSTLAKLI LGLLVAEQGD
IDVFDERLTV ETVHHVRSKI GMVFQNPDNQ FVGATVADDV AFGLENIQVE SSEMPQKIDN
ALTIVGMQEF KNREPHTLSG GQKQRVALAS VLALQPKIII LDEATAMLDP DGRATVMETL
QKLKKQFGKE LTLVTITHDM DEATLADRVV VINDGQKILD GTPAEVFSQR KALHENGLEL
PFANELAFHL NEKPNKYMDE RELIQWLSTL NK
